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Database: PDB
Entry: 8ATC
LinkDB: 8ATC
Original site: 8ATC 
HEADER    TRANSFERASE (CARBAMOYL-P,ASPARTATE)     25-AUG-89   8ATC              
TITLE     COMPLEX OF N-PHOSPHONACETYL-L-ASPARTATE WITH ASPARTATE                
TITLE    2 CARBAMOYLTRANSFERASE. X-RAY REFINEMENT, ANALYSIS OF CONFORMATIONAL   
TITLE    3 CHANGES AND CATALYTIC AND ALLOSTERIC MECHANISMS                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE (R STATE), CATALYTIC CHAIN; 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 EC: 2.1.3.2;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN;           
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   6 ORGANISM_TAXID: 562                                                  
KEYWDS    TRANSFERASE (CARBAMOYL-P, ASPARTATE)                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.KE,W.N.LIPSCOMB,Y.CHO,R.B.HONZATKO                                  
REVDAT   5   14-FEB-24 8ATC    1       REMARK SEQADV LINK                       
REVDAT   4   29-NOV-17 8ATC    1       HELIX                                    
REVDAT   3   24-FEB-09 8ATC    1       VERSN                                    
REVDAT   2   01-APR-03 8ATC    1       JRNL                                     
REVDAT   1   15-OCT-90 8ATC    0                                                
JRNL        AUTH   H.M.KE,W.N.LIPSCOMB,Y.J.CHO,R.B.HONZATKO                     
JRNL        TITL   COMPLEX OF N-PHOSPHONACETYL-L-ASPARTATE WITH ASPARTATE       
JRNL        TITL 2 CARBAMOYLTRANSFERASE. X-RAY REFINEMENT, ANALYSIS OF          
JRNL        TITL 3 CONFORMATIONAL CHANGES AND CATALYTIC AND ALLOSTERIC          
JRNL        TITL 4 MECHANISMS.                                                  
JRNL        REF    J.MOL.BIOL.                   V. 204   725 1988              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   3066911                                                      
JRNL        DOI    10.1016/0022-2836(88)90365-8                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.C.STEVENS,J.E.GOUAUX,W.N.LIPSCOMB                          
REMARK   1  TITL   STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE   
REMARK   1  TITL 2 OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE 
REMARK   1  TITL 3 UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT             
REMARK   1  TITL 4 2.6-ANGSTROMS RESOLUTION                                     
REMARK   1  REF    BIOCHEMISTRY                  V.  29  7691 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.E.GOUAUX,R.C.STEVENS,W.N.LIPSCOMB                          
REMARK   1  TITL   CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED 
REMARK   1  TITL 2 WITH PHOSPHONOACETAMIDE, MALONATE, AND CTP OR ATP AT         
REMARK   1  TITL 3 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH                      
REMARK   1  REF    BIOCHEMISTRY                  V.  29  7702 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.E.GOUAUX,W.N.LIPSCOMB                                      
REMARK   1  TITL   CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND       
REMARK   1  TITL 2 PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF          
REMARK   1  TITL 3 ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION   
REMARK   1  TITL 4 AND NEUTRAL PH                                               
REMARK   1  REF    BIOCHEMISTRY                  V.  29   389 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   J.E.GOUAUX,W.N.LIPSCOMB                                      
REMARK   1  TITL   STRUCTURAL TRANSITIONS IN CRYSTALS OF NATIVE ASPARTATE       
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE                                         
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  86   845 1989              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   J.E.GOUAUX,W.N.LIPSCOMB,S.A.MIDDLETON,E.R.KANTROWITZ         
REMARK   1  TITL   STRUCTURE OF A SINGLE AMINO ACID MUTANT OF ASPARTATE         
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE AT 2.5-ANGSTROMS RESOLUTION.            
REMARK   1  TITL 3 IMPLICATIONS FOR THE COOPERATIVE MECHANISM                   
REMARK   1  REF    BIOCHEMISTRY                  V.  28  1798 1989              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   E.R.KANTROWITZ,W.N.LIPSCOMB                                  
REMARK   1  TITL   ESCHERICHIA COLI ASPARTATE TRANSCARBAMYLASE. THE RELATION    
REMARK   1  TITL 2 BETWEEN STRUCTURE AND FUNCTION                               
REMARK   1  REF    SCIENCE                       V. 241   669 1988              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   J.E.GOUAUX,W.N.LIPSCOMB                                      
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF CARBAMOYL PHOSPHATE AND       
REMARK   1  TITL 2 SUCCINATE BOUND TO ASPARTATE CARBAMOYLTRANSFERASE            
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  85  4205 1988              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 8                                                          
REMARK   1  AUTH   K.H.KIM,Z.PAN,R.B.HONZATKO,H.KE,W.N.LIPSCOMB                 
REMARK   1  TITL   STRUCTURAL ASYMMETRY IN THE CTP-LIGANDED FORM OF ASPARTATE   
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI                   
REMARK   1  REF    J.MOL.BIOL.                   V. 196   853 1987              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 9                                                          
REMARK   1  AUTH   K.L.KRAUSE,K.W.VOLZ,W.N.LIPSCOMB                             
REMARK   1  TITL   2.5 ANGSTROMS STRUCTURE OF ASPARTATE CARBAMOYLTRANSFERASE    
REMARK   1  TITL 2 COMPLEXED WITH THE BISUBSTRATE ANALOG                        
REMARK   1  TITL 3 N-(PHOSPHONACETYL)-L-ASPARTATE                               
REMARK   1  REF    J.MOL.BIOL.                   V. 193   527 1987              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 10                                                         
REMARK   1  AUTH   J.E.GOUAUX,K.L.KRAUSE,W.N.LIPSCOMB                           
REMARK   1  TITL   THE CATALYTIC MECHANISM OF ESCHERICHIA COLI ASPARTATE        
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE. A MOLECULAR MODELLING STUDY            
REMARK   1  REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 142   893 1987              
REMARK   1  REFN                   ISSN 0006-291X                               
REMARK   1 REFERENCE 11                                                         
REMARK   1  AUTH   K.L.KRAUSE,K.W.VOLZ,W.N.LIPSCOMB                             
REMARK   1  TITL   STRUCTURE AT 2.9-ANGSTROMS RESOLUTION OF ASPARTATE           
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE COMPLEXED WITH THE BISUBSTRATE ANALOGUE 
REMARK   1  TITL 3 N-(PHOSPHONACETYL)-L-ASPARTATE                               
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  82  1643 1985              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 12                                                         
REMARK   1  AUTH   H.KE,R.B.HONZATKO,W.N.LIPSCOMB                               
REMARK   1  TITL   STRUCTURE OF UNLIGATED ASPARTATE CARBAMOYLTRANSFERASE OF     
REMARK   1  TITL 2 ESCHERICHIA COLI AT 2.6-ANGSTROMS RESOLUTION                 
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  81  4037 1984              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 13                                                         
REMARK   1  AUTH   R.B.HONZATKO,J.L.CRAWFORD,H.L.MONACO,J.E.LADNER,             
REMARK   1  AUTH 2 B.F.P.EDWARDS,D.R.EVANS,S.G.WARREN,D.C.WILEY,R.C.LADNER,     
REMARK   1  AUTH 3 W.N.LIPSCOMB                                                 
REMARK   1  TITL   CRYSTAL AND MOLECULAR STRUCTURES OF NATIVE AND CTP-LIGANDED  
REMARK   1  TITL 2 ASPARTATE CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI         
REMARK   1  REF    J.MOL.BIOL.                   V. 160   219 1982              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 14                                                         
REMARK   1  AUTH   R.B.HONZATKO,W.N.LIPSCOMB                                    
REMARK   1  TITL   INTERACTIONS OF PHOSPHATE LIGANDS WITH ESCHERICHIA COLI      
REMARK   1  TITL 2 ASPARTATE CARBAMOYLTRANSFERASE IN THE CRYSTALLINE STATE      
REMARK   1  REF    J.MOL.BIOL.                   V. 160   265 1982              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 15                                                         
REMARK   1  AUTH   R.B.HONZATKO,W.N.LIPSCOMB                                    
REMARK   1  TITL   INTERACTIONS OF METAL-NUCLEOTIDE COMPLEXES WITH ASPARTATE    
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE IN THE CRYSTALLINE STATE                
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  79  7171 1982              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 16                                                         
REMARK   1  AUTH   J.E.LADNER,J.P.KITCHELL,R.B.HONZATKO,H.M.KE,K.W.VOLZ,        
REMARK   1  AUTH 2 A.J.KALB(GILBOA),R.C.LADNER,W.N.LIPSCOMB                     
REMARK   1  TITL   GROSS QUATERNARY CHANGES IN ASPARTATE CARBAMOYLTRANSFERASE   
REMARK   1  TITL 2 ARE INDUCED BY THE BINDING OF                                
REMARK   1  TITL 3 N-(PHOSPHONACETYL)-L-ASPARTATE. A 3.5-ANGSTROMS RESOLUTION   
REMARK   1  TITL 4 STUDY                                                        
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  79  3125 1982              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 17                                                         
REMARK   1  AUTH   R.B.HONZATKO,H.L.MONACO,W.N.LIPSCOMB                         
REMARK   1  TITL   A 3.0-ANGSTROMS RESOLUTION STUDY OF NUCLEOTIDE COMPLEXES     
REMARK   1  TITL 2 WITH ASPARTATE CARBAMOYLTRANSFERASE                          
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  76  5105 1979              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 18                                                         
REMARK   1  AUTH   H.L.MONACO,J.L.CRAWFORD,W.N.LIPSCOMB                         
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURES OF ASPARTATE                    
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI AND OF ITS        
REMARK   1  TITL 3 COMPLEX WITH CYTIDINE TRIPHOSPHATE                           
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  75  5276 1978              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 19                                                         
REMARK   1  AUTH   W.N.LIPSCOMB,B.F.P.EDWARDS,D.R.EVANS,S.C.PASTRA-LANDIS       
REMARK   1  TITL   BINDING SITE AT 5.5 ANGSTROMS RESOLUTION OF CYTIDINE         
REMARK   1  TITL 2 TRIPHOSPHATE, THE ALLOSTERIC INHIBITOR OF ASPARTATE          
REMARK   1  TITL 3 TRANSCARBAMYLASE FROM ESCHERICHIA COLI. RELATION TO          
REMARK   1  TITL 4 MECHANISMS OF CONTROL                                        
REMARK   1  EDIT   M.SUNDARALINGAM, S.T.RAO                                     
REMARK   1  REF    STRUCTURE AND CONFORMATION             333 1975              
REMARK   1  REF  2 OF NUCLEIC ACIDS AND                                         
REMARK   1  REF  3 PROTEIN-NUCLEIC ACID                                         
REMARK   1  REF  4 INTERACTIONS : PROCEEDINGS                                   
REMARK   1  REF  5 OF THE FOURTH ANNUAL HARRY                                   
REMARK   1  REF  6 STEENBOCK SYMPOSIUM, JUNE                                    
REMARK   1  REF  7 16-19, 1974, MADISON,                                        
REMARK   1  REF  8 WISCONSIN                                                    
REMARK   1  PUBL   UNIVERSITY PARK PRESS,BALTIMORE                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 20                                                         
REMARK   1  AUTH   S.G.WARREN,B.F.P.EDWARDS,D.R.EVANS,D.C.WILEY,W.N.LIPSCOMB    
REMARK   1  TITL   ASPARTATE TRANSCARBAMOYLASE FROM ESCHERICHIA COLI. ELECTRON  
REMARK   1  TITL 2 DENSITY AT 5.5 ANGSTROMS RESOLUTION                          
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  70  1117 1973              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7106                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 932                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.000 ; 0.014               
REMARK   3    ANGLE DISTANCE                  (A) : 0.000 ; 0.037               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.000 ; 0.055               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.000 ; 0.011               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.100 ; 0.149               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.200 ; 0.206               
REMARK   3    MULTIPLE TORSION                (A) : 0.200 ; 0.243               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.200 ; 0.224               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 2.000 ; 2.100               
REMARK   3    STAGGERED                 (DEGREES) : 17.000; 17.700              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 1.500 ; 1.599               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 2.800 ; 2.815               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 2.300 ; 2.396               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 4.000 ; 4.085               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THERE IS A NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS WHICH                 
REMARK   3  RELATES THE *A* AND *B* CHAINS TO THE *C* AND *D* CHAINS.           
REMARK   4                                                                      
REMARK   4 8ATC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000179961.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 31700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 103800 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.2 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      122.11000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       61.05500            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      105.75036            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     ASN D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     LEU D     7                                                      
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 109   SG                                                     
REMARK 620 2 CYS B 114   SG  110.1                                              
REMARK 620 3 CYS B 138   SG  111.5 111.1                                        
REMARK 620 4 CYS B 141   SG  105.5 108.3 110.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 109   SG                                                     
REMARK 620 2 CYS D 114   SG  112.1                                              
REMARK 620 3 CYS D 138   SG  110.1 104.6                                        
REMARK 620 4 CYS D 141   SG  105.5 111.0 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: PAA                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: PAL binding site                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZNB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: Zinc binding site                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PAC                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: PAL binding site                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZND                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: Zinc binding site                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PAL A 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PAL C 311                 
DBREF  8ATC A    1   310  UNP    P0A786   PYRB_ECOLI       1    310             
DBREF  8ATC B    2   153  UNP    P0A7F3   PYRI_ECOLI       1    152             
DBREF  8ATC C    1   310  UNP    P0A786   PYRB_ECOLI       1    310             
DBREF  8ATC D    2   153  UNP    P0A7F3   PYRI_ECOLI       1    152             
SEQADV 8ATC GLN A   60  UNP  P0A786    GLU    60 CONFLICT                       
SEQADV 8ATC GLN A  147  UNP  P0A786    GLU   147 CONFLICT                       
SEQADV 8ATC GLU A  149  UNP  P0A786    GLN   149 CONFLICT                       
SEQADV 8ATC GLU A  196  UNP  P0A786    GLN   196 CONFLICT                       
SEQADV 8ATC GLY B    8  UNP  P0A7F3    GLN     7 CONFLICT                       
SEQADV 8ATC GLN C   60  UNP  P0A786    GLU    60 CONFLICT                       
SEQADV 8ATC GLN C  147  UNP  P0A786    GLU   147 CONFLICT                       
SEQADV 8ATC GLU C  149  UNP  P0A786    GLN   149 CONFLICT                       
SEQADV 8ATC GLU C  196  UNP  P0A786    GLN   196 CONFLICT                       
SEQADV 8ATC GLY D    8  UNP  P0A7F3    GLN     7 CONFLICT                       
SEQRES   1 A  310  ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN          
SEQRES   2 A  310  ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR          
SEQRES   3 A  310  ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU          
SEQRES   4 A  310  LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER          
SEQRES   5 A  310  THR ARG THR ARG LEU SER PHE GLN THR SER MET HIS ARG          
SEQRES   6 A  310  LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN          
SEQRES   7 A  310  THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR          
SEQRES   8 A  310  ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET          
SEQRES   9 A  310  ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU          
SEQRES  10 A  310  PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY          
SEQRES  11 A  310  SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE          
SEQRES  12 A  310  THR ILE GLN GLN THR GLU GLY ARG LEU ASP ASN LEU HIS          
SEQRES  13 A  310  VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL          
SEQRES  14 A  310  HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN          
SEQRES  15 A  310  ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO          
SEQRES  16 A  310  GLU TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA          
SEQRES  17 A  310  TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU          
SEQRES  18 A  310  VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG          
SEQRES  19 A  310  LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE          
SEQRES  20 A  310  VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN          
SEQRES  21 A  310  MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE          
SEQRES  22 A  310  ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE          
SEQRES  23 A  310  GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU          
SEQRES  24 A  310  LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU                  
SEQRES   1 B  153  MET THR HIS ASP ASN LYS LEU GLY VAL GLU ALA ILE LYS          
SEQRES   2 B  153  ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY          
SEQRES   3 B  153  PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP          
SEQRES   4 B  153  GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU          
SEQRES   5 B  153  MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE          
SEQRES   6 B  153  LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA          
SEQRES   7 B  153  PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL          
SEQRES   8 B  153  VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP          
SEQRES   9 B  153  ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS          
SEQRES  10 B  153  ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG          
SEQRES  11 B  153  ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS          
SEQRES  12 B  153  GLU PHE SER HIS ASN VAL VAL LEU ALA ASN                      
SEQRES   1 C  310  ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN          
SEQRES   2 C  310  ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR          
SEQRES   3 C  310  ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU          
SEQRES   4 C  310  LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER          
SEQRES   5 C  310  THR ARG THR ARG LEU SER PHE GLN THR SER MET HIS ARG          
SEQRES   6 C  310  LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN          
SEQRES   7 C  310  THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR          
SEQRES   8 C  310  ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET          
SEQRES   9 C  310  ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU          
SEQRES  10 C  310  PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY          
SEQRES  11 C  310  SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE          
SEQRES  12 C  310  THR ILE GLN GLN THR GLU GLY ARG LEU ASP ASN LEU HIS          
SEQRES  13 C  310  VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL          
SEQRES  14 C  310  HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN          
SEQRES  15 C  310  ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO          
SEQRES  16 C  310  GLU TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA          
SEQRES  17 C  310  TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU          
SEQRES  18 C  310  VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG          
SEQRES  19 C  310  LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE          
SEQRES  20 C  310  VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN          
SEQRES  21 C  310  MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE          
SEQRES  22 C  310  ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE          
SEQRES  23 C  310  GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU          
SEQRES  24 C  310  LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU                  
SEQRES   1 D  153  MET THR HIS ASP ASN LYS LEU GLY VAL GLU ALA ILE LYS          
SEQRES   2 D  153  ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY          
SEQRES   3 D  153  PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP          
SEQRES   4 D  153  GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU          
SEQRES   5 D  153  MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE          
SEQRES   6 D  153  LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA          
SEQRES   7 D  153  PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL          
SEQRES   8 D  153  VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP          
SEQRES   9 D  153  ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS          
SEQRES  10 D  153  ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG          
SEQRES  11 D  153  ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS          
SEQRES  12 D  153  GLU PHE SER HIS ASN VAL VAL LEU ALA ASN                      
HET    PAL  A 311      16                                                       
HET     ZN  B 154       1                                                       
HET    PAL  C 311      16                                                       
HET     ZN  D 154       1                                                       
HETNAM     PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID                               
HETNAM      ZN ZINC ION                                                         
FORMUL   5  PAL    2(C6 H10 N O8 P)                                             
FORMUL   6   ZN    2(ZN 2+)                                                     
FORMUL   9  HOH   *932(H2 O)                                                    
HELIX    1 H1A ARG A   17  ALA A   32  1                                  16    
HELIX    2 H2A THR A   53  LEU A   66  1                                  14    
HELIX    3 H3A ALA A   89  VAL A   99  1                                  11    
HELIX    4 H4A ALA A  111  SER A  119  1                                   9    
HELIX    5 H5A PRO A  135  GLU A  149  1                                  15    
HELIX    6 H6A ARG A  167  PHE A  179  1                                  13    
HELIX    7 H7A GLU A  196  LYS A  205  1                                  10    
HELIX    8 H8A ILE A  215  ALA A  220  1                                   6    
HELIX    9 H0A ALA A  251  ASN A  256  1                                   6    
HELIX   10 HEA THR A  275  LYS A  279  1                                   5    
HELIX   11 HTA TYR A  285  LEU A  304  1                                  20    
HELIX   12 H1B ILE B   25  PHE B   33  1                                   9    
HELIX   13 H2B ASP B   69  TYR B   77  5ENDS TYPE 1                        9    
HELIX   14 H3B HIS B  147  VAL B  150  1                                   4    
HELIX   15 H1C ARG C   17  ALA C   32  1                                  16    
HELIX   16 H2C THR C   53  LEU C   66  1                                  14    
HELIX   17 H3C ALA C   89  VAL C   99  1                                  11    
HELIX   18 H4C ALA C  111  SER C  119  1                                   9    
HELIX   19 H5C PRO C  135  GLU C  149  1                                  15    
HELIX   20 H6C ARG C  167  PHE C  179  1                                  13    
HELIX   21 H7C GLU C  196  LYS C  205  1                                  10    
HELIX   22 H8C ILE C  215  ALA C  220  1                                   6    
HELIX   23 H0C ALA C  251  ASN C  256  1                                   6    
HELIX   24 HEC THR C  275  LYS C  279  1                                   5    
HELIX   25 HTC TYR C  285  LEU C  304  1                                  20    
HELIX   26 H1D ILE D   25  PHE D   33  1                                   9    
HELIX   27 H2D ASP D   69  TYR D   77  5ENDS TYPE 1                        9    
HELIX   28 H3D HIS D  147  VAL D  150  1                                   4    
SHEET    1 C1A 5 LYS A   7  ILE A   9  0                                        
SHEET    2 C1A 5 PRO A 123  ALA A 127  1                                        
SHEET    3 C1A 5 ALA A 101  HIS A 106  1                                        
SHEET    4 C1A 5 LYS A  42  PHE A  48  1                                        
SHEET    5 C1A 5 ALA A  68  SER A  74  1                                        
SHEET    1 C2A 6 ALA A 208  HIS A 212  0                                        
SHEET    2 C2A 6 ASN A 182  ALA A 188  1                                        
SHEET    3 C2A 6 LEU A 155  VAL A 160  1                                        
SHEET    4 C2A 6 ILE A 224  VAL A 230  1                                        
SHEET    5 C2A 6 LYS A 262  HIS A 265  1                                        
SHEET    6 C2A 6 PRO A 281  ALA A 283  1                                        
SHEET    1 R1B 5 ARG B  41  LEU B  46  0                                        
SHEET    2 R1B 5 ARG B  55  GLU B  62 -1                                        
SHEET    3 R1B 5 ARG B  14  ASP B  19 -1                                        
SHEET    4 R1B 5 THR B  82  ASP B  87 -1                                        
SHEET    5 R1B 5 GLY B  93  PRO B  97 -1                                        
SHEET    1 R2B 4 GLU B 101  ASP B 104  0                                        
SHEET    2 R2B 4 SER B 123  LYS B 129 -1                                        
SHEET    3 R2B 4 ILE B 134  CYS B 138 -1                                        
SHEET    4 R2B 4 LYS B 143  SER B 146 -1                                        
SHEET    1 C1C 5 LYS C   7  ILE C   9  0                                        
SHEET    2 C1C 5 PRO C 123  ALA C 127  1                                        
SHEET    3 C1C 5 ALA C 101  HIS C 106  1                                        
SHEET    4 C1C 5 LYS C  42  PHE C  48  1                                        
SHEET    5 C1C 5 ALA C  68  SER C  74  1                                        
SHEET    1 C2C 6 ALA C 208  HIS C 212  0                                        
SHEET    2 C2C 6 ASN C 182  ALA C 188  1                                        
SHEET    3 C2C 6 LEU C 155  VAL C 160  1                                        
SHEET    4 C2C 6 ILE C 224  VAL C 230  1                                        
SHEET    5 C2C 6 LYS C 262  HIS C 265  1                                        
SHEET    6 C2C 6 PRO C 281  ALA C 283  1                                        
SHEET    1 R1D 5 ARG D  41  LEU D  46  0                                        
SHEET    2 R1D 5 ARG D  55  GLU D  62 -1                                        
SHEET    3 R1D 5 ARG D  14  ASP D  19 -1                                        
SHEET    4 R1D 5 THR D  82  ASP D  87 -1                                        
SHEET    5 R1D 5 GLY D  93  PRO D  97 -1                                        
SHEET    1 R2D 4 GLU D 101  ASP D 104  0                                        
SHEET    2 R2D 4 SER D 123  LYS D 129 -1                                        
SHEET    3 R2D 4 ILE D 134  CYS D 138 -1                                        
SHEET    4 R2D 4 LYS D 143  SER D 146 -1                                        
LINK         SG  CYS B 109                ZN    ZN B 154     1555   1555  2.06  
LINK         SG  CYS B 114                ZN    ZN B 154     1555   1555  2.05  
LINK         SG  CYS B 138                ZN    ZN B 154     1555   1555  2.04  
LINK         SG  CYS B 141                ZN    ZN B 154     1555   1555  2.06  
LINK         SG  CYS D 109                ZN    ZN D 154     1555   1555  2.05  
LINK         SG  CYS D 114                ZN    ZN D 154     1555   1555  2.07  
LINK         SG  CYS D 138                ZN    ZN D 154     1555   1555  2.10  
LINK         SG  CYS D 141                ZN    ZN D 154     1555   1555  2.02  
CISPEP   1 LEU A  267    PRO A  268          0         2.15                     
CISPEP   2 LEU C  267    PRO C  268          0         2.60                     
SITE     1 PAA  9 SER A  52  ARG A  54  THR A  55  SER A  80                    
SITE     2 PAA  9 LYS A  84  HIS A 134  ARG A 167  ARG A 229                    
SITE     3 PAA  9 GLN A 231                                                     
SITE     1 ZNB  4 CYS B 109  CYS B 114  CYS B 138  CYS B 141                    
SITE     1 PAC  9 SER C  52  ARG C  54  THR C  55  SER C  80                    
SITE     2 PAC  9 LYS C  84  HIS C 134  ARG C 167  ARG C 229                    
SITE     3 PAC  9 GLN C 231                                                     
SITE     1 ZND  4 CYS D 109  CYS D 114  CYS D 138  CYS D 141                    
SITE     1 AC1  4 CYS B 109  CYS B 114  CYS B 138  CYS B 141                    
SITE     1 AC2  4 CYS D 109  CYS D 114  CYS D 138  CYS D 141                    
SITE     1 AC3 16 SER A  52  THR A  53  ARG A  54  THR A  55                    
SITE     2 AC3 16 SER A  80  LYS A  84  ARG A 105  HIS A 134                    
SITE     3 AC3 16 ARG A 167  THR A 168  ARG A 229  GLN A 231                    
SITE     4 AC3 16 LEU A 267  HOH A 330  HOH A 337  HOH A 367                    
SITE     1 AC4 15 SER C  52  THR C  53  ARG C  54  THR C  55                    
SITE     2 AC4 15 SER C  80  LYS C  84  ARG C 105  HIS C 134                    
SITE     3 AC4 15 GLN C 137  ARG C 167  ARG C 229  GLN C 231                    
SITE     4 AC4 15 LEU C 267  HOH C 329  HOH C 331                               
CRYST1  122.110  122.110  156.170  90.00  90.00 120.00 P 3 2 1      12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008189  0.004728  0.000000        0.00000                         
SCALE2      0.000000  0.009456  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006403        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system